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  • Drosophila  (737)
  • Springer  (737)
  • Nature Publishing Group
  • 1
    Electronic Resource
    Electronic Resource
    Searching for a Common Centromeric Structural Motif: Drosophila Centromeric Satellite DNAs Show Propensity to form Telomeric-Like Unusual DNA Structures (2000)
    Springer
    Genetica 109 (2000), S. 71-75 
    Details
    ISSN: 1573-6857
    Keywords: centromere ; heterochromatin ; non B-DNA structures ; Drosophila
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The molecular basis of centromere formation in a particular chromosomal region is not yet understood. In higher eukaryotes, no specific DNA sequence is required for the assembly of the kinetochore, but similar centromeric chromatins are formed on different centromere DNA sequences. Although epigenesis has been proposed as the main mechanism for centromere specification, DNA recognition must also play a role. Through the analysis of Drosophilacentromeric DNA sequences, we found that dodeca satellite and 18HT satellite are able to form unusual DNA structures similar to those formed by telomeric sequences. These findings suggest the existence of a common centromeric structural DNA motif which we feel merits further investigation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026546510127
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  • 2
    Electronic Resource
    Electronic Resource
    A maximum likelihood statistical method for analyzing frequency-dependent fitness experiments (1979)
    Springer
    Behavior genetics 9 (1979), S. 7-21 
    Details
    ISSN: 1573-3297
    Keywords: frequency-dependent fitness ; statistical analysis ; logistic regression models ; maximum likelihood estimation ; Drosophila
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Psychology
    Notes: Abstract Experiments on frequency-dependent fitness often consist of forming pairwise mixtures of distinguishable types at several frequency combinations. These mixtures are allowed to undergo competition, after which the performance of each type is enumerated. A statistical method for analyzing such experiments is described in this article. This method, suggested previously for other purposes, is superior to the statistical procedures now commonly employed. It involves the maximum likelihood estimation of parameters for two logistic regression models: one which assumes that fitness is frequency-dependent, the other that fitness is constant over changing frequency. Estimators for both models can be calculated without difficulty using an iterative numerical algorithm implemented in a Fortran computer program available from the authors. Fitting both models allows for the construction of a likelihood ratio statistical test for whichever model is more appropriate. The method is illustrated by application to publishedDrosophila data from differential mating success experiments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01067118
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  • 3
    Electronic Resource
    Electronic Resource
    Positional information in imaginal discs transformed by homoeotic mutations (1978)
    Springer
    Development genes and evolution 185 (1978), S. 271-292 
    Details
    ISSN: 1432-041X
    Keywords: Homeotic mutations ; Imaginal disc ; Positional Information ; Drosophila
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations of the bithorax complex result in segmental transformations in the thorax and abdomen ofDrosophila. The haltere discs from larvae homozygous forbx 3 orpbx are transformed so that the discs contain cells that will produce wing cuticle as well as cells that produce haltere cuticle. The pattern regulation behavior of these discs has been examined. The fate maps of the two discs were established, and then the regulative behavior of a number of fragments from both types of mutant discs was established by culturing the fragments in vivo prior to metamorphosis. The most important conclusion from this work is that the cells producing, haltere cuticle and wing cuticle within the same disc share the same positional information and that they communicate during pattern regulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00848356
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  • 4
    Electronic Resource
    Electronic Resource
    The spatial expression ofDrosophila rotund gene reveals that the imaginal discs are organized in domains along the proximal-distal axis (1992)
    Springer
    Development genes and evolution 201 (1992), S. 284-295 
    Details
    ISSN: 1432-041X
    Keywords: Drosophila ; Imaginal discs ; Pattern formation ; rotund
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary InDrosophila imaginal discs, pattern formation requires the activity of three positional information systems, antero-posterior (A/P), dorso-ventral (D/V) and proximo-distal (P/D). Three genes,Decapentaplegic, Distal-less androtund (rn), involved in pattern formation along the P/D axis have been characterized. Thern gene is required in a sub-distal region, localized at a similar position along the P/D axis in all appendages; it encodes two major transcripts, m1.7 and m5.3, both expressed in the central region of all the major imaginal discs. The present study of these transcripts in severalrn mutant favours m5.3 as encodingrn morphogenetic function in the imaginal discs. The fine characterization of its distribution partitions all major imaginal discs in domains along the P/D axis. The ventral and dorsal discs appear to be similarly but not identically organized: two P/D domains are evident in the wing and haltere discs whilst the leg and antenna discs appear to be composed of at least three. We also show that m5.3 is sex-regulated in the genital disc and thatrn function is required for proper development of a sub-distal structure of the female genitalia. This suggests that the primordia of the female genitalia may be organized in a similar way to the other imaginal discs, and strongly supports the hypothesis thatrn function is specific to pattern formation along the P/D axis and that it may be involved in the establishment or maintenance of this pattern.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00592109
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  • 5
    Electronic Resource
    Electronic Resource
    Drosophila hemolymph proteins: Purification, characterization, and genetic mapping of larval serum protein 2 in D. melanogaster (1978)
    Springer
    Biochemical genetics 16 (1978), S. 101-119 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila ; hemolymph proteins ; gene regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Three of the major protein species present in the hemolymph of Drosophila melanogaster larvae just prior to pupation are absent from second instar larvae but accumulate rapidly during the third instar. This article describes the purification and characterization of one of these, larval serum protein (LSP) 2, using an immunological assay. It is a homohexamer of molecular weight about 450,000, with a polypeptide molecular weight of 78,000–83,000. Fast and slow electrophoretic variants of this protein map between the markers vin and gs, at 36–37 on chromosome 3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484387
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  • 6
    Electronic Resource
    Electronic Resource
    Adaptation ofDrosophila enzymes to temperature. III. Evolutionary conservatism in mitochondrial enzymes (1980)
    Springer
    Journal of molecular evolution 16 (1980), S. 37-46 
    Details
    ISSN: 1432-1432
    Keywords: Evolution ; Drosophila ; Temperature ; Mitochondrial enzymes ; Kinetic properties
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The evolutionary behavior of two mitochondrial enzymes (L-glycerol 3-phosphate:cytochrome c oxidoreductase E.C.1.1.1.95,αGPO, and L-malate: NAD+ oxidoreductase, E.C.1.1.1.37, m-MDH) obtained from several temperate and tropicalDrosophila species was examined by comparing their catalytic properties, which related to temperature (Km-Ea-Q10-Thermostability). MitochondrialαGPO or m-MDH obtained either from temperate or from tropical species was found to exhibit similar catalytic properties while for both cytosolic enzymes, theαGPDH and s-MDH, Km patterns were similar among species from the same thermal habitat and different between thermal habitats. In combination with other observations reported in the literature these facts support the view that the function, and probably the structure, of mitochondrial enzymes are better conserved in evolution than those of the corresponding enzymes found in the cytosol. It is proposed that the relative invariance of the mitochondrial enzymes structure is probably linked to a necessary relative invariance of molecular interactions inside the mitochondrion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01732068
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  • 7
    Electronic Resource
    Electronic Resource
    Drosophila lactate dehydrogenase: Developmental aspects (1983)
    Springer
    Biochemical genetics 21 (1983), S. 199-211 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila ; lactate dehydrogenase ; isozymic pattern ; development ; isozymic conversion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Partially purified lactate dehydrogenase (LDH) from third-instar larvae displays two bands (one major and one minor) on polyacrylamide gels. Analogous preparations from pupae and adults exhibit three LDH-staining bands (one major and two minor) in a similar pattern. The migration of the major band is similar for larvae, pupae, and adults, while the two minor LDH bands of pupae and adults migrate more slowly than the minor larval band. It has been shown that larval LDH incubated with β-nicotinamide adenine dinucleotide exhibits two additional minor bands with an electrophoretic mobility similar to that of the minor bands of both pupae and adults. The intensity of the minor larval LDH band (exhibited also by untreated preparations) is drastically reduced. This fact indicates that the life-cycle stage-dependent LDH isozymic distribution is possibly due to a posttranslational effect(s). Highly purified LDH from larvae, pupae, or adults, obtained by an affinity chromatography procedure, displays just one dispersed band, located in the area between the band 5 and the band 6 exhibited by crude extract preparations. These data, in combination with the lack of difference in catalytic properties among enzymes from larvae, pupae, and adults, suggest that LDH synthesis is controlled by the same single structural gene at all developmental stages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02395404
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  • 8
    Electronic Resource
    Electronic Resource
    Drosophila lactate dehydrogenase: Developmental aspects (1983)
    Springer
    Biochemical genetics 21 (1983), S. 199-211 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila ; lactate dehydrogenase ; isozymic pattern ; development ; isozymic conversion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Partially purified lactate dehydrogenase (LDH) from third-instar larvae displays two bands (one major and one minor) on polyacrylamide gels. Analogous preparations from pupae and adults exhibit three LDH-staining bands (one major and two minor) in a similar pattern. The migration of the major band is similar for larvae, pupae, and adults, while the two minor LDH bands of pupae and adults migrate more slowly than the minor larval band. It has been shown that larval LDH incubated with β-nicotinamide adenine dinucleotide exhibits two additional minor bands with an electrophoretic mobility similar to that of the minor bands of both pupae and adults. The intensity of the minor larval LDH band (exhibited also by untreated preparations) is drastically reduced. This fact indicates that the life-cycle stage-dependent LDH isozymic distribution is possibly due to a posttranslational effect(s). Highly purified LDH from larvae, pupae, or adults, obtained by an affinity chromatography procedure, displays just one dispersed band, located in the area between the band 5 and the band 6 exhibited by crude extract preparations. These data, in combination with the lack of difference in catalytic properties among enzymes from larvae, pupae, and adults, suggest that LDH synthesis is controlled by the same single structural gene at all developmental stages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00000018
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  • 9
    Electronic Resource
    Electronic Resource
    Thermal stability of α-glycerophosphate dehydrogenase in Drosophila (1981)
    Springer
    Biochemical genetics 19 (1981), S. 311-320 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila ; thermal stability of enzyme ; α-glycerophosphate dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Thermal stability of α-glycerophosphate dehydrogenase-1 (α-Gpdh-1) in nine Drosophila species was studied at pH's ranging from 6.4 to 8.5. This was done by measuring the changes in the activity of enzymes during the heat denaturation process. In addition to temperature, the rate of denaturation is highly dependent on the pH of the incubation buffer. The results of this study show that the thermal stability of enzyme molecules is different in different species. This holds true also in the species in which the enzymes have been found to be identical by other means. The differences between species of the Drosophila virilis group are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504276
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  • 10
    Electronic Resource
    Electronic Resource
    Analysis of nucleotide substitutions and amino acid conservation in theDrosophila Adh genomic region (1994)
    Springer
    Genetica 94 (1994), S. 27-36 
    Details
    ISSN: 1573-6857
    Keywords: Adh ; Adh-dup ; Drosophila ; molecular clock ; nucleotide substitution rates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The homologous genomic region that contains two paralogous genes,Adh andAdh-dup, was compared in severalDrosophila species. Sequences were analyzed as follows: a) At the nucleotide level, Ka and Ks values were determined for each pair of species. Ka-Adh and Ka-Adh-dup are not significantly different. However, Ks-Adh values are significantly lower than Ks-Adh-dup, which are more variable. In agreement with other reports, lower Ks values forAdh correlate with a high level of gene expression and relatively high percentage of G+C content in the third codon position, while the opposite applies toAdh-dup. b) At the protein level, amino acid comparisons reveal conserved regions shared by ADH and ADH-DUP, which have been assigned to known functional domains. Key residues for dehydrogenasic function are also found in ADH-DUP, thus pointing to a dehydrogenase activity for ADH-DUP, albeit very different from that of ADH.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01429217
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